1czt

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[[Image:1czt.gif|left|200px]]
[[Image:1czt.gif|left|200px]]
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{{Structure
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{{STRUCTURE_1czt| PDB=1czt | SCENE= }}
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|RELATEDENTRY=[[1czs|1CZS]], [[1czv|1CZV]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1czt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1czt OCA], [http://www.ebi.ac.uk/pdbsum/1czt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1czt RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V'''
'''CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V'''
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[[Category: Kane, W H.]]
[[Category: Kane, W H.]]
[[Category: Macedo-Ribeiro, S.]]
[[Category: Macedo-Ribeiro, S.]]
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[[Category: blood clotting]]
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[[Category: Blood clotting]]
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[[Category: calcium-independent]]
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[[Category: Calcium-independent]]
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[[Category: coagulation]]
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[[Category: Coagulation]]
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[[Category: discoidin family]]
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[[Category: Discoidin family]]
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[[Category: membrane-binding]]
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[[Category: Membrane-binding]]
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Revision as of 10:17, 2 May 2008

Template:STRUCTURE 1czt

CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V


Overview

Rapid and controlled clot formation is achieved through sequential activation of circulating serine proteinase precursors on phosphatidylserine-rich procoagulant membranes of activated platelets and endothelial cells. The homologous complexes Xase and prothrombinase, each consisting of an active proteinase and a non-enzymatic cofactor, perform critical steps within this coagulation cascade. The activated cofactors VIIIa and Va, highly specific for their cognate proteinases, are each derived from precursors with the same A1-A2-B-A3-C1-C2 architecture. Membrane binding is mediated by the C2 domains of both cofactors. Here we report two crystal structures of the C2 domain of human factor Va. The conserved beta-barrel framework provides a scaffold for three protruding loops, one of which adopts markedly different conformations in the two crystal forms. We propose a mechanism of calcium-independent, stereospecific binding of factors Va and VIIIa to phospholipid membranes, on the basis of (1) immersion of hydrophobic residues at the apices of these loops in the apolar membrane core; (2) specific interactions with phosphatidylserine head groups in the groove enclosed by these loops; and (3) favourable electrostatic contacts of basic side chains with negatively charged membrane phosphate groups.

About this Structure

1CZT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of the membrane-binding C2 domain of human coagulation factor V., Macedo-Ribeiro S, Bode W, Huber R, Quinn-Allen MA, Kim SW, Ortel TL, Bourenkov GP, Bartunik HD, Stubbs MT, Kane WH, Fuentes-Prior P, Nature. 1999 Nov 25;402(6760):434-9. PMID:10586886 Page seeded by OCA on Fri May 2 13:17:14 2008

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